ISSN:
1573-6881
Keywords:
Terminal oxidase
;
redox coupling
;
electrochemical gradient
;
electron transport
;
energy transduction
;
proton translocation
;
crystal structure
;
site-directed mutagenesis
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract One of the challenging features of energy-transducing terminal oxidases, like the aa 3 cytochrome c oxidase of Paracoccus denitrificans, is the translocation of protons across the cytoplasmic membrane, which is coupled to the transfer of electrons to oxygen. As a prerequisite for a more advanced examination of the enzymatic properties, several amino acid residues, selected on the basis of recent three-dimensional structure determinations, were exchanged in subunit I of the Paracoccus enzyme by site-directed mutagenesis. The properties of the mutated oxidases were analyzed by different methods to elucidate whether they are involved in the coupled and coordinated transfer of protons via two different pathways either to the site of oxygen reduction or through the enzyme from the cytoplasm to the periplasmic side.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1020515713103
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